Abstract:
:Amyotrophic lateral sclerosis (ALS) is a fatal motor neuron disease, whose primary mechanisms or causes are still not defined and for which no effective treatment is available. We have recently reported that before disease onset the level of tyrosine nitrated proteins is increased in the G93A SOD1 transgenic mouse model of ALS. In the present investigation, we carried out a proteomic analysis of spinal cord extracts from G93A SOD1 mice at the presymptomatic stage of the disease to further unravel primary events in the pathogenesis and tentatively screen for potential pharmacological targets. Using a robust two-dimensional gel electrophoresis-based proteomic approach, we detected a number of proteins differentially represented in presymptomatic mice in comparison with controls. Alterations of these proteins correlate with mitochondrial dysfunction, aggregation, and stress response. Moreover, we found a variation in the isoform pattern of cyclophilin A, a molecular chaperone that protects cells from the oxidative stress.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Massignan T,Casoni F,Basso M,Stefanazzi P,Biasini E,Tortarolo M,Salmona M,Gianazza E,Bendotti C,Bonetto Vdoi
10.1016/j.bbrc.2006.12.075subject
Has Abstractpub_date
2007-02-16 00:00:00pages
719-25issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(06)02752-5journal_volume
353pub_type
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